ID A0A2U1VLR3_9PROT Unreviewed; 889 AA.
AC A0A2U1VLR3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TSO221_29895 {ECO:0000313|EMBL:PWC35386.1};
OS Azospirillum sp. TSO22-1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=716789 {ECO:0000313|EMBL:PWC35386.1, ECO:0000313|Proteomes:UP000245126};
RN [1] {ECO:0000313|EMBL:PWC35386.1, ECO:0000313|Proteomes:UP000245126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSO22-1 {ECO:0000313|EMBL:PWC35386.1,
RC ECO:0000313|Proteomes:UP000245126};
RA Jang J., Ishii S.;
RT "Comparative genome analysis of Azospirillum sp. strains.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWC35386.1}.
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DR EMBL; LGQZ01000144; PWC35386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1VLR3; -.
DR Proteomes; UP000245126; Unassembled WGS sequence.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; NF041832; near_NosP_CTERM; 1.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF12860; PAS_7; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000245126}.
FT DOMAIN 349..419
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 419..474
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 531..744
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 767..884
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 66..100
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 462..524
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 818
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 889 AA; 98876 MW; 6BC4E195A5765D36 CRC64;
MIRGGPGEDP PDDVEGLRAE VARLRRVNDA LMDHVERSMN LGGNSFALFQ TASLLEQQVR
RRTLELETAL HDIEQTNREL SAATRSLETA QNRLTDALEA ISDGFVLCDS DGGIVIFNST
FHALWRGVGD LLRPGVPFQQ LIARATERGL IRESAEARRW LARRSDGRQR RNTHVLEMAD
GRWLRISERP THENGFVGIY SDITAIKTQE RRRRERELAA KSTLLQATLD NLSQGVSVFN
ADLELVAWNH RLTELLDLPE GRLRAGAPLA SFLALPAVRR PFADDGREPE ALVRWLKSTR
SIPTRSLELD CPDGRTLEVR SNPMPDGGFV TTFADITHLR RSEAALRDSE WRIRLVTDAI
PARIAYLDRD ERYQFTNRAY EDWIGRTRTE IAGQRLRDLL TPEQYALRRP YTARVLAGES
CEFDMTTPAA NGETAYVHAV YVPHRAPDGE TVLGFFSLLQ DVTESKRAAA QLEEANRMLE
ERVAQRTRAL TELNDKLRAE IGERIAAEEA MRRAKAEAEQ ANLSKTKFLA AASHDLLQPM
NAARVFVAAL AERRLGRHNM ALVDNITESL EAVDDLLNTL LDLSKLDAGV LPMHVTDFRI
EPLLRQLATQ FSPLAEQRGL EFRVVPSGAV VRSDMALLGR ILRNFLSNAV RYTPTGRVLL
GCRRTPTGLR IGVADTGIGI PADKTQEIFI EFHRLKGSRS SRDCGAGLGL AIVDRIARRL
DHPIHVQSTF GRGSVFAVEV PYGSADRIEA PHPAAIRSEA GSLKGVSVLL IENEPTILAA
MAALMHEWGC ELIHGDGADA VLPLIAERPD AIDVVIADYH LDEGRIGIDA LQAVRKRCGR
TVPGIIITAD RSDEVLARVK AHGLHLLTKP IKPAHLRSLL VHLRSRRSE
//
